XYLG_PSEPU
ID XYLG_PSEPU Reviewed; 486 AA.
AC P23105;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=2-hydroxymuconic semialdehyde dehydrogenase;
DE Short=HMSD;
DE EC=1.2.1.85;
GN Name=xylG;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OG Plasmid TOL pWW0.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1791759; DOI=10.1111/j.1365-2958.1991.tb02091.x;
RA Horn J.M., Harayama S., Timmis K.N.;
RT "DNA sequence determination of the TOL plasmid (pWWO) xylGFJ genes of
RT Pseudomonas putida: implications for the evolution of aromatic
RT catabolism.";
RL Mol. Microbiol. 5:2459-2474(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PAO;
RX PubMed=1339433; DOI=10.1016/s0021-9258(18)42252-1;
RA Steele M.I., Lorenz D., Hatter K., Park A., Sokatch J.R.;
RT "Characterization of the mmsAB operon of Pseudomonas aeruginosa PAO
RT encoding methylmalonate-semialdehyde dehydrogenase and 3-hydroxyisobutyrate
RT dehydrogenase.";
RL J. Biol. Chem. 267:13585-13592(1992).
RN [3]
RP PROTEIN SEQUENCE OF 1-15, AND CATALYTIC ACTIVITY.
RX PubMed=7868591; DOI=10.1128/jb.177.5.1196-1201.1995;
RA Inoue J., Shaw J.P., Rekik M., Harayama S.;
RT "Overlapping substrate specificities of benzaldehyde dehydrogenase (the
RT xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the
RT xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida.";
RL J. Bacteriol. 177:1196-1201(1995).
CC -!- FUNCTION: 2-hydroxymuconic acid semialdehyde can be converted to 2-
CC hydroxypent-2,4-dienoate either directly by the action of 2-
CC hydroxymuconic semialdehyde hydrolase (HMSH) or by the action of three
CC sequential enzymes, the first of which is HMSD. Can oxidize not only 2-
CC hydroxymuconic semialdehyde and its analogs but also benzaldehyde and
CC its analogs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O + NAD(+) =
CC (2Z,4E)-2-hydroxyhexa-2,4-dienedioate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:34219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28080, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:71198; EC=1.2.1.85;
CC Evidence={ECO:0000269|PubMed:7868591};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.3 for the oxidation of 2-hydroxymuconic semialdehyde,
CC and 9.6 for that of benzaldehyde.;
CC -!- PATHWAY: Aromatic compound metabolism; benzoate degradation via
CC hydroxylation.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; M64747; AAA26053.1; -; Genomic_DNA.
DR PIR; E42902; E42902.
DR RefSeq; NP_542865.1; NC_003350.1.
DR RefSeq; WP_011005908.1; NC_003350.1.
DR AlphaFoldDB; P23105; -.
DR SMR; P23105; -.
DR KEGG; ag:AAA26053; -.
DR BioCyc; MetaCyc:MON-3402; -.
DR UniPathway; UPA00156; -.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0043640; P:benzoate catabolic process via hydroxylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR017628; OHmuconic_semiald_DH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR03216; OH_muco_semi_DH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; NAD;
KW Oxidoreductase; Plasmid.
FT CHAIN 1..486
FT /note="2-hydroxymuconic semialdehyde dehydrogenase"
FT /id="PRO_0000056594"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 288
FT /evidence="ECO:0000250"
FT CONFLICT 11..12
FT /note="EL -> AF (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 51761 MW; 854303F121B2FFBD CRC64;
MKEIKHFISG ELVGSASGKL FDNVSPANGQ VIGRVHEAGR AEVDAAVRAA RAALKGPWGK
MTVAERAEIL HRVADGITAR FGEFLEARMP GHRQAEVAGQ PHRHSARRAN FKVFADLLKN
VANEAFEMAT PDGAGALNYG VRRPKGVIGV ISPWNLPLLL MTWKVGPALA CGNCVVVKPS
EETPLTATLL GEVMQAAGVP AGVYNVVHGF GGDSAGAFLT EHPDVDAYTF TGETGTGETI
MRAAAKGVRQ VSLELGGKNA GIVFADCDMD KAIEGTLRSA FANCGQVCLG TERVYVERPI
FDAFVARLKA GAEALKIGEP NDPEANFGPL ISHKPREKVP SYYQQAVDDG ATVVTGGGVP
EMPAHLAGGA WVQPTIWTGL ADDSAVVTEE IFGPCCHIRP FDSEEEAIEL ANSLPYGLAS
AIWTENVRRA HRVAGQIEAG IVWVNSWFLR DLRTAFGGSK QSGIGREGGV HSLEFYTELK
NICVKL